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Database: PDB
Entry: 4EHQ
LinkDB: 4EHQ
Original site: 4EHQ 
HEADER    PROTEIN BINDING                         03-APR-12   4EHQ              
TITLE     CRYSTAL STRUCTURE OF CALMODULIN BINDING DOMAIN OF ORAI1 IN COMPLEX    
TITLE    2 WITH CA2+/CALMODULIN DISPLAYS A UNIQUE BINDING MODE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CALCIUM RELEASE-ACTIVATED CALCIUM CHANNEL PROTEIN 1;       
COMPND   8 CHAIN: G;                                                            
COMPND   9 SYNONYM: PROTEIN ORAI-1, TRANSMEMBRANE PROTEIN 142A;                 
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CAM3, CAMC;  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    CALMODULIN, ORAI1, CALCIUM DEPENDENT INACTIVATION, EF HAND, CALCIUM   
KEYWDS   2 BINDING, CALCIUM-DEPENDENT INACTIVATION, CALMODULIN BINDING DOMAIN   
KEYWDS   3 OF ORAI1, NONE, CYTOSOL, PROTEIN BINDING                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LIU,X.ZHENG,G.A.MUELLER,M.SOBHANY,E.F.DEROSE,Y.ZHANG,R.E.LONDON,    
AUTHOR   2 L.BIRNBAUMER                                                         
REVDAT   3   02-JAN-13 4EHQ    1       JRNL                                     
REVDAT   2   14-NOV-12 4EHQ    1       JRNL                                     
REVDAT   1   07-NOV-12 4EHQ    0                                                
JRNL        AUTH   Y.LIU,X.ZHENG,G.A.MUELLER,M.SOBHANY,E.F.DEROSE,Y.ZHANG,      
JRNL        AUTH 2 R.E.LONDON,L.BIRNBAUMER                                      
JRNL        TITL   CRYSTAL STRUCTURE OF CALMODULIN BINDING DOMAIN OF ORAI1 IN   
JRNL        TITL 2 COMPLEX WITH CA2+*CALMODULIN DISPLAYS A UNIQUE BINDING MODE. 
JRNL        REF    J.BIOL.CHEM.                  V. 287 43030 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23109337                                                     
JRNL        DOI    10.1074/JBC.M112.380964                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 11118                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 524                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.9877 -  3.0143    0.98     2887   132  0.1883 0.2148        
REMARK   3     2  3.0143 -  2.3938    0.97     2766   125  0.1824 0.2391        
REMARK   3     3  2.3938 -  2.0916    0.98     2728   144  0.1573 0.1936        
REMARK   3     4  2.0916 -  1.9005    0.80     2213   123  0.1647 0.2169        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 44.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.94820                                              
REMARK   3    B22 (A**2) : -0.67420                                             
REMARK   3    B33 (A**2) : -0.27400                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.69510                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           1443                                  
REMARK   3   ANGLE     :  0.879           1991                                  
REMARK   3   CHIRALITY :  0.064            210                                  
REMARK   3   PLANARITY :  0.003            251                                  
REMARK   3   DIHEDRAL  : 13.077            581                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071632.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : COPPER ANODE                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11497                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1IWQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.0, 40% PPG P400,     
REMARK 280  14% BUTYROLACTONE, 1% N-OCTYL-BETA-D-GLUCOPYRANOSIDE, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.03700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       12.35450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.03700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       12.35450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   2    CG   OD1  OD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A   41   OE1                                                 
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 TYR A  99   O    81.9                                              
REMARK 620 3 ASN A  97   OD1  89.5  83.0                                        
REMARK 620 4 GLU A 104   OE1 100.8  80.3 158.9                                  
REMARK 620 5 ASP A  95   OD1  82.4 151.1  72.8 126.5                            
REMARK 620 6 GLU A 104   OE2  94.9 131.6 145.5  52.7  73.9                      
REMARK 620 7 HOH A 316   O   173.9  94.5  85.2  83.4  98.8  91.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 GLN A 135   O    85.4                                              
REMARK 620 3 ASP A 131   OD1  81.1 154.3                                        
REMARK 620 4 GLU A 140   OE1 108.3  80.0 125.1                                  
REMARK 620 5 ASP A 133   OD1  86.5  76.3  81.1 150.8                            
REMARK 620 6 GLU A 140   OE2  90.7 128.2  74.0  52.5 155.1                      
REMARK 620 7 HOH A 304   O   164.5  99.4  88.7  87.0  80.4  97.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 THR A  62   O    88.1                                              
REMARK 620 3 ASN A  60   OD1  91.5  79.8                                        
REMARK 620 4 GLU A  67   OE1 101.0  83.3 158.7                                  
REMARK 620 5 ASP A  58   OD1  76.6 149.2  74.1 125.5                            
REMARK 620 6 GLU A  67   OE2  85.8 131.9 148.0  51.5  74.2                      
REMARK 620 7 HOH A 356   O   159.8 111.3  86.7  87.4  83.6  85.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  24   OD1  81.2                                              
REMARK 620 3 THR A  26   O    80.0  77.8                                        
REMARK 620 4 GLU A  31   OE2  99.4 157.0 125.1                                  
REMARK 620 5 ASP A  22   OD1  85.0  81.6 156.1  75.6                            
REMARK 620 6 GLU A  31   OE1 110.7 148.8  76.2  52.4 126.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBL A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBL A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBL A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBL G 101                 
DBREF  4EHQ A    1   148  UNP    P62161   CALM_RAT         2    149             
DBREF  4EHQ G   69    88  UNP    Q96D31   CRCM1_HUMAN     69     88             
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 G   20  HIS SER MET GLN ALA LEU SER TRP ARG LYS LEU TYR LEU          
SEQRES   2 G   20  SER ARG ALA LYS LEU LYS ALA                                  
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HET    GBL  A 205      12                                                       
HET    GBL  A 206      12                                                       
HET    GBL  A 207      12                                                       
HET    GBL  G 101      12                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GBL GAMMA-BUTYROLACTONE                                              
HETSYN     GBL DIHYDROFURAN-2(3H)-ONE                                           
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  GBL    4(C4 H6 O2)                                                  
FORMUL  11  HOH   *88(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 ASP A   64  ASP A   93  1                                  30    
HELIX    5   5 SER A  101  LEU A  112  1                                  12    
HELIX    6   6 THR A  117  ASP A  129  1                                  13    
HELIX    7   7 TYR A  138  THR A  146  1                                   9    
HELIX    8   8 SER G   75  LYS G   87  1                                  13    
SHEET    1   A 2 TYR A  99  ILE A 100  0                                        
SHEET    2   A 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  93                CA    CA A 203     1555   1555  2.30  
LINK         OD1 ASP A 129                CA    CA A 202     1555   1555  2.30  
LINK         OD1 ASP A  56                CA    CA A 204     1555   1555  2.32  
LINK         O   TYR A  99                CA    CA A 203     1555   1555  2.33  
LINK         OD1 ASP A  20                CA    CA A 201     1555   1555  2.35  
LINK         O   THR A  62                CA    CA A 204     1555   1555  2.35  
LINK         O   GLN A 135                CA    CA A 202     1555   1555  2.36  
LINK         OD1 ASN A  97                CA    CA A 203     1555   1555  2.36  
LINK         OE1 GLU A 104                CA    CA A 203     1555   1555  2.38  
LINK         OD1 ASP A  24                CA    CA A 201     1555   1555  2.38  
LINK         OD1 ASN A  60                CA    CA A 204     1555   1555  2.38  
LINK         O   THR A  26                CA    CA A 201     1555   1555  2.38  
LINK         OD1 ASP A 131                CA    CA A 202     1555   1555  2.40  
LINK         OE1 GLU A 140                CA    CA A 202     1555   1555  2.40  
LINK         OD1 ASP A 133                CA    CA A 202     1555   1555  2.41  
LINK         OD1 ASP A  95                CA    CA A 203     1555   1555  2.42  
LINK         OE2 GLU A  31                CA    CA A 201     1555   1555  2.45  
LINK         OE1 GLU A  67                CA    CA A 204     1555   1555  2.45  
LINK         OD1 ASP A  22                CA    CA A 201     1555   1555  2.50  
LINK         OE2 GLU A 140                CA    CA A 202     1555   1555  2.52  
LINK         OE1 GLU A  31                CA    CA A 201     1555   1555  2.52  
LINK         OE2 GLU A 104                CA    CA A 203     1555   1555  2.54  
LINK         OD1 ASP A  58                CA    CA A 204     1555   1555  2.54  
LINK         OE2 GLU A  67                CA    CA A 204     1555   1555  2.59  
LINK        CA    CA A 203                 O   HOH A 316     1555   1555  2.37  
LINK        CA    CA A 204                 O   HOH A 356     1555   1555  2.41  
LINK        CA    CA A 202                 O   HOH A 304     1555   1555  2.44  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 306                                          
SITE     1 AC2  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC2  6 GLU A 140  HOH A 304                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 316                                          
SITE     1 AC4  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC4  6 GLU A  67  HOH A 356                                          
SITE     1 AC5  6 GLU A  45  ALA A  46  GLY A  98  TYR A  99                    
SITE     2 AC5  6 ASN A 137  HOH A 369                                          
SITE     1 AC6  4 GLU A  45  PHE A  89  TYR A 138  HOH A 327                    
SITE     1 AC7  6 ALA A  57  PRO A  66  GLU A  67  THR A  70                    
SITE     2 AC7  6 LYS G  78  HOH G 206                                          
SITE     1 AC8  7 MET A 109  LEU A 112  GLU A 114  LEU G  74                    
SITE     2 AC8  7 LYS G  78  LEU G  79  SER G  82                               
CRYST1  100.074   24.709   60.903  90.00 100.10  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009993  0.000000  0.001779        0.00000                         
SCALE2      0.000000  0.040471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016678        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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